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The VigilMovie 2019



DevOps Research and Assessment (DORA), a pioneer in helping organizations achieve high DevOps and organizational performance with data-driven insights, and Google Cloud are excited to announce the launch of the 2019 Accelerate State of DevOps Report. The report provides a comprehensive view of the DevOps industry, providing actionable guidance for organizations of all sizes and in all industries to improve their software delivery performance to ultimately become an elite DevOps performer. With six years of research and data from more than 31,000 professionals worldwide, the 2019 Accelerate State of DevOps Report is the largest and longest-running research of its kind.




The VigilMovie | 2019



Thanks to everyone who contributed to the survey. We hope this report helps organizations of all sizes, industries, and regions improve. We look forward to hearing your thoughts and feedback on the report. Here are some ways you can learn more about 2019 The Accelerate State of DevOps Report.


On July 30, 2019, CBO reposted the file of long-term budget projections to include additional data for the percentage of population growth attributable to births, deaths, and net immigration. In the same file, CBO also corrected values for earnings as a share of compensation.


This report outlines the key findings of the 2019 Point-In-Time (PIT) count and Housing Inventory Count (HIC) conducted in January 2019. Specifically, this report provides 2019 national, state, and CoC-level PIT and HIC estimates of homelessness, as well as estimates of chronically homeless persons, homeless veterans, and homeless children and youth.


A mysterious outbreak of atypical pneumonia in late 2019 was traced to a seafood wholesale market in Wuhan of China. Within a few weeks, a novel coronavirus tentatively named as 2019 novel coronavirus (2019-nCoV) was announced by the World Health Organization. We performed bioinformatics analysis on a virus genome from a patient with 2019-nCoV infection and compared it with other related coronavirus genomes. Overall, the genome of 2019-nCoV has 89% nucleotide identity with bat SARS-like-CoVZXC21 and 82% with that of human SARS-CoV. The phylogenetic trees of their orf1a/b, Spike, Envelope, Membrane and Nucleoprotein also clustered closely with those of the bat, civet and human SARS coronaviruses. However, the external subdomain of Spike's receptor binding domain of 2019-nCoV shares only 40% amino acid identity with other SARS-related coronaviruses. Remarkably, its orf3b encodes a completely novel short protein. Furthermore, its new orf8 likely encodes a secreted protein with an alpha-helix, following with a beta-sheet(s) containing six strands. Learning from the roles of civet in SARS and camel in MERS, hunting for the animal source of 2019-nCoV and its more ancestral virus would be important for understanding the origin and evolution of this novel lineage B betacoronavirus. These findings provide the basis for starting further studies on the pathogenesis, and optimizing the design of diagnostic, antiviral and vaccination strategies for this emerging infection.


The outbreak of a novel coronavirus (2019-nCoV) represents a pandemic threat that has been declared a public health emergency of international concern. The CoV spike (S) glycoprotein is a key target for vaccines, therapeutic antibodies, and diagnostics. To facilitate medical countermeasure development, we determined a 3.5-angstrom-resolution cryo-electron microscopy structure of the 2019-nCoV S trimer in the prefusion conformation. The predominant state of the trimer has one of the three receptor-binding domains (RBDs) rotated up in a receptor-accessible conformation. We also provide biophysical and structural evidence that the 2019-nCoV S protein binds angiotensin-converting enzyme 2 (ACE2) with higher affinity than does severe acute respiratory syndrome (SARS)-CoV S. Additionally, we tested several published SARS-CoV RBD-specific monoclonal antibodies and found that they do not have appreciable binding to 2019-nCoV S, suggesting that antibody cross-reactivity may be limited between the two RBDs. The structure of 2019-nCoV S should enable the rapid development and evaluation of medical countermeasures to address the ongoing public health crisis.


Stream and share the recording of the 2019 National School Climate Survey webinar! In this webinar, we present new findings from the 2019 NSCS about the school experiences of LGBTQ youth, discuss how school climate has changed over the past twenty years for LGBTQ students since we first began conducting the NSCS, and respond to questions from webinar viewers. Originally broadcast on October 14, 2020.


Stream and share our webinar on the experiences of transgender and nonbinary students! Using data from the 2019 National School Climate Survey, we examine what school is like for transgender and nonbinary students, how their experiences are distinct from those of cisgender LGBQ students, and how school experiences differ among different transgender and nonbinary students. We also examine the school policies that can make a difference in the lives of transgender and nonbinary students.


After collecting and processing 3207 micrograph movies, we obtained a 3.5-Å-resolution three-dimensional (3D) reconstruction of an asymmetrical trimer in which a single RBD was observed in the up conformation. (Fig. 1B, fig. S2, and table S1). Because of the small size of the RBD (21 kDa), the asymmetry of this conformation was not readily apparent until ab initio 3D reconstruction and classification were performed (Fig. 1B and fig. S3). By using the 3D variability feature in cryoSPARC v2 (15), we observed breathing of the S1 subunits as the RBD underwent a hinge-like movement, which likely contributed to the relatively poor local resolution of S1 compared with the more stable S2 subunit (movies S1 and S2). This seemingly stochastic RBD movement has been captured during structural characterization of the closely related betacoronaviruses SARS-CoV and MERS-CoV, as well as the more distantly related alphacoronavirus porcine epidemic diarrhea virus (PEDV) (10, 11, 13, 16). The observation of this phenomenon in 2019-nCoV S suggests that it shares the same mechanism of triggering that is thought to be conserved among the Coronaviridae, wherein receptor binding to exposed RBDs leads to an unstable three-RBD up conformation that results in shedding of S1 and refolding of S2 (11, 12).


The overall structure of 2019-nCoV S resembles that of SARS-CoV S, with a root mean square deviation (RMSD) of 3.8 Å over 959 Cα atoms (Fig. 2A). One of the larger differences between these two structures (although still relatively minor) is the position of the RBDs in their respective down conformations. Whereas the SARS-CoV RBD in the down conformation packs tightly against the N-terminal domain (NTD) of the neighboring protomer, the 2019-nCoV RBD in the down conformation is angled closer to the central cavity of the trimer (Fig. 2B). Despite this observed conformational difference, when the individual structural domains of 2019-nCoV S are aligned to their counterparts from SARS-CoV S, they reflect the high degree of structural homology between the two proteins, with the NTDs, RBDs, subdomains 1 and 2 (SD1 and SD2), and S2 subunits yielding individual RMSD values of 2.6 Å, 3.0 Å, 2.7 Å, and 2.0 Å, respectively (Fig. 2C).


(A) Single protomer of 2019-nCoV S with the RBD in the down conformation (left) is shown in ribbons colored according to Fig. 1. A protomer of 2019-nCoV S in the RBD up conformation is shown (center) next to a protomer of SARS-CoV S in the RBD up conformation (right), displayed as ribbons and colored white (PDB ID: 6CRZ). (B) RBDs of 2019-nCoV and SARS-CoV aligned based on the position of the adjacent NTD from the neighboring protomer. The 2019-nCoV RBD is colored green and the SARS-CoV RBD is colored white. The 2019-nCoV NTD is colored blue. (C) Structural domains from 2019-nCoV S have been aligned to their counterparts from SARS-CoV S as follows: NTD (top left), RBD (top right), SD1 and SD2 (bottom left), and S2 (bottom right).


(A) Surface plasmon resonance sensorgram showing the binding kinetics for human ACE2 and immobilized 2019-nCoV S. Data are shown as black lines, and the best fit of the data to a 1:1 binding model is shown in red. (B) Negative-stain EM 2D class averages of 2019-nCoV S bound by ACE2. Averages have been rotated so that ACE2 is positioned above the 2019-nCoV S protein with respect to the viral membrane. A diagram depicting the ACE2-bound 2019-nCoV S protein is shown (right) with ACE2 in blue and S protein protomers colored tan, pink, and green.


(A) SARS-CoV RBD shown as a white molecular surface (PDB ID: 2AJF), with residues that vary in the 2019-nCoV RBD colored red. The ACE2-binding site is outlined with a black dashed line. (B) Biolayer interferometry sensorgram showing binding to ACE2 by the 2019-nCoV RBD-SD1. Binding data are shown as a black line, and the best fit of the data to a 1:1 binding model is shown in red. (C) Biolayer interferometry to measure cross-reactivity of the SARS-CoV RBD-directed antibodies S230, m396, and 80R. Sensor tips with immobilized antibodies were dipped into wells containing 2019-nCoV RBD-SD1, and the resulting data are shown as a black line.


Figure 4. (A,B) Detrended anomalies of ERA5 monthly sea level pressure (SLP, shading) and surface winds (arrows) from September to October 2019. The anomalies are calculated relative to the period January 1982 and April 2020.


Figure 10. Hovmøller diagram of detrended monthly anomalies of SST (shading), SLA (contours), and surface winds (arrows) averaged between 0E and 10E from August 2019 to March 2020. Anomalies are computed relative to the period January 1982 and April 2020. 041b061a72


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